Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation
about
A strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome cThe Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA EnzymesOxidation State-dependent Protein-Protein Interactions in Disulfide CascadesIron Binding at Specific Sites within the Octameric HbpS Protects Streptomycetes from Iron-Mediated Oxidative StressStructural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter pyloriDiversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.CCS5, a thioredoxin-like protein involved in the assembly of plastid c-type cytochromesHelicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231.Characterization of ResDE-dependent fnr transcription in Bacillus subtilis.2-nitrobenzoate 2-nitroreductase (NbaA) switches its substrate specificity from 2-nitrobenzoic acid to 2,4-dinitrobenzoic acid under oxidizing conditionsReduced reliance on the trace element selenium during evolution of mammals.Ischemia-reperfusion and cardioprotection: a delicate balance between reactive oxygen species generation and redox homeostasis.Ion Torrent-based transcriptional assessment of a Corynebacterium pseudotuberculosis equi strain reveals denaturing high-performance liquid chromatography a promising rRNA depletion method.Cytochrome c biogenesis: the Ccm system.Composition and function of cytochrome c biogenesis System II.ROS-Mediated Signalling in Bacteria: Zinc-Containing Cys-X-X-Cys Redox Centres and Iron-Based Oxidative Stress.Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.The active-site cysteinyls and hydrophobic cavity residues of ResA are important for cytochrome c maturation in Bacillus subtilisBiochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for meningococcal viability.Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency.Membrane-spanning and periplasmic segments of CcmI have distinct functions during cytochrome c Biogenesis in Rhodobacter capsulatus.Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation.Impact of selected amino acids of HP0377 (Helicobacter pylori thiol oxidoreductase) on its functioning as a CcmG (cytochrome c maturation) protein and Dsb (disulfide bond) isomerase.
P2860
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P2860
Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation
description
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name
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@ast
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@en
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@nl
type
label
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@ast
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@en
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@nl
prefLabel
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@ast
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@en
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@nl
P2093
P2860
P356
P1476
Mechanism of substrate specifi ...... ved in cytochrome c maturation
@en
P2093
Christopher L Colbert
Paul J A Erbel
P2860
P304
P356
10.1073/PNAS.0600552103
P407
P577
2006-03-13T00:00:00Z